Lin Jason Ching-Yao, Chiang Bing-Yu, Chou Chi-Chi, Chen Tzu-Chieh, Chen Yi-Ju, Chen Yu-Ju, Lin Chun-Hung
Institute of Biological Chemistry, Academia Sinica, 128 Academia Road Section 2, Taipei 11529, Taiwan.
Institute of Chemistry, Academia Sinica, 128 Academia Road Section 2, Taipei 11529, Taiwan.
Molecules. 2015 Jan 15;20(1):1452-74. doi: 10.3390/molecules20011452.
Cysteine is very susceptible to reactive oxygen species. In response; posttranslational thiol modifications such as reversible disulfide bond formation have arisen as protective mechanisms against undesired in vivo cysteine oxidation. In Gram-negative bacteria a major defense mechanism against cysteine overoxidation is the formation of mixed protein disulfides with low molecular weight thiols such as glutathione and glutathionylspermidine. In this review we discuss some of the mechanistic aspects of glutathionylspermidine in prokaryotes and extend its potential use to eukaryotes in proteomics and biochemical applications through an example with tissue transglutaminase and its S-glutathionylation.
半胱氨酸极易受到活性氧的影响。作为应对措施，翻译后硫醇修饰（如可逆二硫键的形成）已成为针对体内半胱氨酸意外氧化的保护机制。在革兰氏阴性菌中，对抗半胱氨酸过度氧化的主要防御机制是与低分子量硫醇（如谷胱甘肽和谷胱甘肽亚精胺）形成混合蛋白二硫键。在本综述中，我们讨论了谷胱甘肽亚精胺在原核生物中的一些作用机制，并通过组织转谷氨酰胺酶及其S-谷胱甘肽化的例子，将其在蛋白质组学和生化应用中的潜在用途扩展到真核生物。
